Chemical Approach to New Conversion of Hemoprotein Function

用人工合成的假体重组肌红蛋白是一种将新的化学功能引入蛋白质的独特方法。在这个项目中，我们提出了两种重构方法，以创建肌红蛋白的新功能。一种是修饰血红素-丙酸侧链，另一种是修饰血红素骨架。我们最近的成果总结如下：在蛋白表面通过人工界面构建蛋白-蛋白复合物；如. .重组肌红蛋白-细胞色素c复合物在人工蛋白复合物内监测光致电子转移。这是解释生物系统中复杂电子传递机制的一个合适模型。在肌红蛋白表面添加底物结合位点后，重组肌红蛋白表现出过氧化物酶和/或过氧合酶的活性。2个血红素-丙酸侧链在肌红蛋白中的作用被用缺少一个丙酸的特殊血红素重组的新肌红蛋白所证实。发现用铁卟啉重组的肌红蛋白表现出极高的双氧亲和力。结果表明，重组方法将作为一种新的方式，在创建一个独特的功能化血红蛋白。

The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. In this project, we proposed two approach to the reconstitutional method in order to create a new function into myoglobin. One is the modification of heme-propionate side chains, and another is the modification of heme framework. The summary of our recent results are shown as follows :1. Protein-protein complex via an artificial interface on the protein surface was constructed ; e.g.. reconstituted myoglobin - cytochrome c complex.2. Photoinduced electron transfer was monitored within the artificial protein complexes. It is a suitable model to elucidate the mechanism of the complicated electron transfer in biological systems.3. Reconstituted myoglobin exhibits peroxidase and/or peroxygenase activities upon the addition of substrate binding site on the myoglobin surface.4. The role of two heme-propionate side chains in the myoglobin was proved by new myoglobin reconstituted with the special heme lacking one of the propionates.5. It is found that myoglobin reconstituted with iron porphycene shows extremely high dioxygen affinity.The net results demonstrate that the reconstitutional method will serve as a new way in the creation of a unique functionalized hemoprotein.